Imperial College London
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Dr Poh-Choo Pang

Faculty of Natural Sciences, Department of Life Sciences

Visiting Researcher
 
 
 
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Contact

 

p.pang05 Website

 
 
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Location

 

Room 3158 Prince's GateSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Yoon:2010:10.3892/ijo_00000490,
author = {Yoon, S-J and Park, S-Y and Pang, P-C and Gallagher, J and Gottesman, JE and Dell, A and Kim, J-H and Hakomori, S-I},
doi = {10.3892/ijo_00000490},
journal = {International Journal of Oncology},
pages = {193--203},
title = {N-glycosylation status of beta-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases},
url = {http://dx.doi.org/10.3892/ijo_00000490},
volume = {36},
year = {2010}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - N-glycosylation status of purified β-haptoglobin separated from sera of patients with prostate cancer was studied in comparison to that of sera from patients with benign prostate diseases, or normal subjects. Two different approaches, as summarized below, one based on binding of lectins and antibodies to β-haptoglobin, the other on mass spectrometry of released N-linked glycans from β-haptoglobin, were performed. Some of the results were useful for distinction of prostate cancer vs. benign prostate diseases. i) Binding of Phaseolus vulgaris-L lectin (PHA-L), defining the GlcNAcβ6Manα6Man side chain present in tri- or tetra-antennary N-linked glycans, to β-haptoglobin was higher for cases of prostate cancer and high-grade prostate intraepithelial neoplasia than for benign diseases. Binding of Aleuria aurantia lectin (AAL) defining Fucα3-, α4-, or α6-GlcNAc, or monoclonal antibody directed to sialyl-Lex, to β-haptoglobin was also higher for some of the cancer cases than for benign diseases. Many other lectins and antibodies showed no binding to β-haptoglobin, or showed no significant difference between cancer vs. benign diseases. ii) Mass spectrometric analysis of N-linked glycans of β-haptoglobin released by Peptide N-glycosidase-F showed enhanced expression of monosialyl tri-antennary structures in prostate cancer cases. Thus, binding of PHA-L to affinity-purified β-haptoglobin from sera of patients could lead to development of useful tools for differential diagnosis of prostate cancer vs. benign prostate diseases.
AU  - Yoon,S-J
AU  - Park,S-Y
AU  - Pang,P-C
AU  - Gallagher,J
AU  - Gottesman,JE
AU  - Dell,A
AU  - Kim,J-H
AU  - Hakomori,S-I
DO  - 10.3892/ijo_00000490
EP  - 203
PY  - 2010///
SN  - 1019-6439
SP  - 193
TI  - N-glycosylation status of beta-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases
T2  - International Journal of Oncology
UR  - http://dx.doi.org/10.3892/ijo_00000490
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000272877100021&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/49847
VL  - 36
ER  -
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